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Molecular mechanism of the binding of neuropeptide achatin-I (Gly-D-Phe-Ala-Asp) to large unilamellar vesicles of zwitterionic egg-yolk phosphatidylcholine (EPC) was investigated by means of natural-abundance 13C and high-resolution (of 0.01Hz order) 1H NMR spectroscopy. The binding equilibrium was found to be sensitive to the ionization state of the N-terminal NH3+ group in achatin-I; the de-ionization...
Sequence-position dependence of the side-chain conformational equilibrium of aspartic acid (Asp) residue is investigated for both model Asp peptides (di- to tetra-) and neuropeptide achatin-I (Gly-D-Phe-Ala-Asp) in aqueous solution. The trans-to-gauche conformational changes on the dihedral angle of C–Cα–Cβ–C are analyzed in terms of the standard free energy ΔG0, enthalpy ΔH0, and entropy −TΔS0. The...
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